Other Enzymes

The numerous separations reported in the literature include surfactants, inorganic ions, enzymes, other proteins, other organics, biological cells, and various other particles and substances. The scale of the systems ranges from the simple Grits test for the presence of surfactants in water, which has been shown to operate by virtue of transient foam fractionation [Lemlich, J. Colloid Interface Sci., 37, 497 (1971)], to the natural adsubble processes that occur on a grand scale in the ocean [Wallace and Duce, Deep Sea Res., 25, 827 (1978)]. For further information see the reviews cited earlier. 

Allosteric site Site on the enzyme other than the active site to which a nonsubstate compound binds. This may result in a conformational change at the active site so that the normal substrate cannot bind to it. 

Whole-cell Systems and Enzymes other than Lipases in Ionic Liquids... 

This is the rate law for many catalyzed reactions, including those catalyzed by enzymes. Other aspects of this subject will be presented in Section 4.7. Here we simply show how [A] varies with time. The variables can be separated, giving the equation... 

The compounds of the t/block elements show a wide range of interesting properties. Some are vital to life. Iron is an essential component of mammalian blood. Compounds of cobalt, molybdenum, and zinc are found in vitamins and essential enzymes. Other compounds simply make life more interesting and colorful. The beautiful color of cobalt blue glass, the brilliant greens and blues of kiln-baked pottery, and many pigments used by artists make use of d-block compounds. 

By enzymatic means, chitosan can be easily depolymerized by a variety of hydrolases including lysozyme, pectinase, cellulases, hemicellulases, lipases and amylases, among others, thus showing a peculiar vulnerability to enzymes other than chitosanases [71-76]. While pectinase is of particular... 

Within the cytoplasm are a number of important subeellular particles whieh include the ribosome and oxy- and deoxyribonucleic acids. Enzymes other than those in the membrane are also present in the eytoplasm. 

Antipsychotic Major CYP450 Metabolic Enzyme Other CYP450 Metabolic Pathways Increase Antipsychotic Concentrations Decrease Antipsychotic Concentrations... 

It is a well-known fact that specific plastic materials like flexible PVC, Polyurethane or Silicone may be easily attacked by microorganisms leading to discoloration or mechanical failures.14 This susceptibility to microbial attack is mainly attributed to the plasticiser content of the material as well as other ingredients such as stabiliser or antioxidants.5,6 The predominant organisms on the surface of those plastics are fungi and actinomycetes and it is said that by the action of their extracellular enzymes other organisms such as bacteria may be able to grow on the material.7... 

So little is known about molybdenum enzymes other than milk xanthine oxidase that there is little to be said by way of general conclusions. In all cases where there is direct evidence (except possibly for xanthine dehydrogenase from Micrococcus lactilyticus) it seems that molybdenum in the enzymes does have a redox function in catalysis. For the xanthine oxidases and dehydrogenases and for aldehyde oxidase, the metal is concerned in interaction of the enzymes with reducing substrates. However, for nitrate reductase it is apparently in interaction with the oxidizing substrate that the metal is involved. In nitrogenase the role of molybdenum is still quite uncertain. 

The work of Eddowes and Hill and Taniguchi and co-workers opened up an extremely exciting prospect, the more as it appeared that the technique of surface modification could be extended to enzymes other than cytochrome c. However, to exploit this technology fully the mode of action of these... 

Biosensors with enzymes other than SODs... 

Luminometric assay of ATP can also be applied to measurement of other substrates such as ADP, AMP, and ATP-specific enzymes. Other examples are reported in Table 4. 

CL reaction can be catalyzed by enzymes other than HRP (e.g., microperoxidase and catalase) and by other substances [hemoglobin, cytochrome c, Fe(III), and other metal complexes]. The presence of suitable molecules such as phenols (p-iodophenol), naphthols (l-bromo-2-naphthol), or amines (p-anisidine) increases the light production deriving from the HRP-catalyzed oxidation of luminol and produces glow-type kinetics [6, 7], The use of other enzymes, such as glucose-6-phosphate dehydrogenase [38-41], P-galactosidase [42], and xanthine oxidase [43-46], as CL labels has been reported. 

The biochemical reactions of living cells are controlled by enzymes, which are defined as temperature-sensitive, organic catalysts. Chemically, the enzymes are proteins that are specific in that they will act as catalysts to accelerate specific reactions. Some of these enzymes are associated with the protoplasm of the cell and perform their function within the cell. They are called intracellular enzymes. Other enzymes are excreted by the cell into the surrounding medium and are known as extracellular enzymes. 

It is possible that, by present techniques, enzymes other than Gal-l-P-uridyl tranferase make an appreciable contribution to the consumption of UDPG or oxygen. 

Show that the value of K agrees with that independently found spectrally (in absence of enzyme). Other cysteine-containing proteins should give a similar pattern and value for K. 

As the first committed step in the biosynthesis of AMP from IMP, AMPSase plays a central role in de novo purine nucleotide biosynthesis. A 6-phosphoryl-IMP intermediate appears to be formed during catalysis, and kinetic studies of E. coli AMPSase demonstrated that the substrates bind to the enzyme active sites randomly. With mammalian AMPSase, aspartate exhibits preferred binding to the E GTPTMP complex rather than to the free enzyme. Other kinetic data support the inference that Mg-aspartate complex formation occurs within the adenylosuccinate synthetase active site and that such a... 

Finally, yet another issue enters into the interpretation of nonlinear Arrhenius plots of enzyme-catalyzed reactions. As is seen in the examples above, one typically plots In y ax (or. In kcat) versus the reciprocal absolute temperature. This protocol is certainly valid for rapid equilibrium enzymes whose rate-determining step does not change throughout the temperature range studied (and, in addition, remains rapid equilibrium throughout this range). However, for steady-state enzymes, other factors can influence the interpretation of the nonlinear data. For example, for an ordered two-substrate, two-product reaction, kcat is equal to kskjl ks + k ) in which ks and k are the off-rate constants for the two products. If these two rate constants have a different temperature dependency (e.g., ks > ky at one temperature but not at another temperature), then a nonlinear Arrhenius plot may result. See Arrhenius Equation Owl Transition-State Theory van t Hoff Relationship... 

This enzyme [EC 3.4.13.3] (also referred to as Xaa-His dipeptidase, X-His dipeptidase, aminoacylhistidine dipeptidase, and homocarnosinase), is a zinc-dependent dipeptidase that catalyzes the hydrolysis of Xaa-His dipeptides. Carnosine, homocarnosine, and anserine are preferred substrates for this mammalian cytosolic enzyme. Other aminoacylhistidine dipeptides are weaker substrates (including homoanserine). The enzyme is activated by thiols and inhibited by metal-chelating agents. O. W. Griffith (1986) Ann. Rev. Biochem. 55, 855. 

The core-enzymes, prepared in our laboratory, and containing the active centers, were successfully crystallized (Dr. Jones, Uppsala, communicated) and tertiary structures will be described in the near future. Chemical modification studies on these enzymes are currently being undertaken in our laboratory identification of important catalytic residues and location of the active centers will lead to more functional information on these enzymes. Other cellulases such as some endoglucanases from Clostridium thermocel-lum (EG A, EG B, EG D) (10) and EngA and Exg from Cellulomonas fimi (19) also contain sequences of conserved, terminally located and sometimes reiterated, amino acids. Some of these sequences are preceded by proline-serine rich domains. Thus, a bistructural-bifunctional organization seems to be a rather common feature among cellulases, at least for EngA and Exg from C. fimi and the enzymes from Trichoderma reesei. 

In soils, electrons are produced by the metabolic activity of soil biota. These electrons are usually accepted by O2 dissolved in the soil solution which is then replaced by O2 from the soil air. Oxygen may, however, become deficient if all pores are filled with water as in waterlogged or compacted soils. Fe in Fe oxides may then function as an alternative electron acceptor and Fe ions will be formed according to eq. (16.3). The electrons are transferred from the decomposing biomass to the Fe oxide by microbially produced enzymes. Other potential electron acceptors in soils are nitrate, Mn and sulphate. 

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